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https://en.wikipedia.org/wiki/4-hydroxyacetophenone%20monooxygenase | In enzymology, a 4-hydroxyacetophenone monooxygenase () is an enzyme that catalyzes the chemical reaction:
(4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 O-acetylhydroquinone + NADP+ + H2O
The 4 substrates of this enzyme are (4-hydroxyphenyl)ethan-1-one, NADPH, H+, and O2, whereas its 3 products are hydroquinone acetate ester, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (4-hydroxyphenyl)ethan-1-one,NADPH:oxygen oxidoreductase (ester-forming). This enzyme is also called HAPMO. This enzyme participates in bisphenol a degradation.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxybenzoate%201-hydroxylase | In enzymology, a 4-hydroxybenzoate 1-hydroxylase () is an enzyme that catalyzes the chemical reaction
4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 hydroquinone + NAD(P)+ + H2O + CO2
The 5 substrates of this enzyme are 4-hydroxybenzoate, NADH, NADPH, H+, and O2, whereas its 5 products are hydroquinone, NAD+, NADP+, H2O, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating). This enzyme is also called 4-hydroxybenzoate 1-monooxygenase. This enzyme participates in 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxybenzoate%203-monooxygenase | The enzyme 4-hydroxybenzoate 3-monooxygenase, also commonly referred to as para-hydroxybenzoate hydroxylase (PHBH), is a flavoprotein belonging to the family of oxidoreductases. Specifically, it is a hydroxylase, and is one of the most studied enzymes and catalyzes reactions involved in soil detoxification, metabolism, and other biosynthetic processes.
4-hydroxybenzoate 3-monooygenase catalyzes the regioselective hydroxylation of 4-hydroxybenzoate, giving 3,4-dihydroxybenzoate as the product. The mechanism consists of the following general steps: (1) reduction of the flavin, (2) reaction of the flavin with O2, producing C4a-hydroperoxyflavin, and (3) binding and activation of the substrate, leading to product formation and release. Throughout the mechanism, the flavin changes between “open” and “closed” conformations, thus altering the substrate reaction environment. The open conformation allows solvent access to the active site; the enzyme adopts this conformation for substrate binding and product release. A closed conformation isolates the reaction from solvent, which helps to stabilize the reaction intermediates.
Structure
4-hydroxybenzoate 3-monooxygenase is a homodimer with a flavin bound to each monomer. The active site is composed of the flavin and amino acids on the monomer. The structure of this enzyme often serves as a model for structure-reactivity interdependence of other flavin-dependent hydroxylases. The active site limits potential substrates to substituted |
https://en.wikipedia.org/wiki/4-hydroxybenzoate%203-monooxygenase%20%28NAD%28P%29H%29 | In enzymology, a 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] () is an enzyme that catalyzes the chemical reaction
4-hydroxybenzoate + NAD(P)H + H+ + O2 3,4-dihydroxybenzoate + NAD(P)+ + H2O
The 5 substrates of this enzyme are 4-hydroxybenzoate, NADH, NADPH, H+, and O2, whereas its 4 products are 3,4-dihydroxybenzoate, NAD+, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating). Other names in common use include 4-hydroxybenzoate 3-monooxygenase (reduced nicotinamide adenine, dinucleotide (phosphate)), 4-hydroxybenzoate-3-hydroxylase, and 4-hydroxybenzoate 3-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxyphenylacetaldehyde%20oxime%20monooxygenase | In enzymology, a 4-hydroxyphenylacetaldehyde oxime monooxygenase () is an enzyme that catalyzes the chemical reaction
(Z)-4-hydroxyphenylacetaldehyde oxime + NADPH + H+ + O2 (S)-4-hydroxymandelonitrile + NADP+ + 2 H2O
The 4 substrates of this enzyme are (Z)-4-hydroxyphenylacetaldehyde oxime, NADPH, H+, and O2, whereas its 3 products are (S)-4-hydroxymandelonitrile, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (Z)-4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase. Other names in common use include 4-hydroxybenzeneacetaldehyde oxime monooxygenase, cytochrome P450II-dependent monooxygenase, NADPH-cytochrome P450 reductase (CYP71E1), CYP71E1, and 4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase. This enzyme participates in tyrosine metabolism.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxyphenylacetate%201-monooxygenase | In enzymology, a 4-hydroxyphenylacetate 1-monooxygenase () is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylacetate + NAD(P)H + H+ + O2 homogentisate + NAD(P)+ + H2O
The 5 substrates of this enzyme are 4-hydroxyphenylacetate, NADH, NADPH, H+, and O2, whereas its 4 products are homogentisate, NAD+, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating). Other names in common use include 4-hydroxyphenylacetate 1-hydroxylase, 4-hydroxyphenylacetic 1-hydroxylase, and 4-HPA 1-hydroxylase. This enzyme participates in tyrosine metabolism.. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-Hydroxyphenylacetate%203-monooxygenase | 4-hydroxyphenylacetate 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylacetate + FADH2 + O2 3,4-dihydroxyphenylacetate + FAD + H2O
This reaction is the first step in a pathway found in enteric bacteria such as Escherichia coli and soil bacteria such as Pseudomonas putida which degrades 4-hydroxyphenylacetate (4-HPA), allowing these bacteria to use 4-HPA and other aromatic compounds found in mammalian digestive tracts or in soil as a carbon source. While most known flavin monooxygenases use NADH or NADPH as substrates (and use the flavins FAD or FMN as prosthetic groups ), this enzyme is part of a two-component system, in which a flavin oxidoreductase partner () regenerates FADH2 by oxidizing NADH to NAD+. hpaB and hpaC, the 4-HPA oxygenase and reductase partner proteins (respectively) of E. coli strain W, were the first two-component flavin monoxygenase system identified. While known examples of this enzyme share a common catalytic mechanism and likely evolutionary origin, they differ with respect to regulation and ability to substitute FMNH2 for FADH2 as a substrate.
Structure
This enzyme is a tetramer which forms as a dimer of dimers. Sequence alignments of the Thermus thermophilus and E. coli hpaB enzymes show structural similarity to each other and to the oxygenase components of other bacterial two-component monooxygenases for compounds such as phenol and chlorophenol. Each monomer of this protein consists of an N-terminal alpha- |
https://en.wikipedia.org/wiki/4-hydroxyquinoline%203-monooxygenase | In enzymology, a 4-hydroxyquinoline 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
quinolin-4-ol + NADH + H+ + O2 quinolin-3,4-diol + NAD+ + H2O
The 4 substrates of this enzyme are quinolin-4-ol, NADH, H+, and O2, whereas its 3 products are quinolin-3,4-diol, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is quinolin-4(1H)-one,NADH:oxygen oxidoreductase (3-oxygenating). This enzyme is also called quinolin-4(1H)-one 3-monooxygenase.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-methoxybenzoate%20monooxygenase%20%28O-demethylating%29 | In enzymology, a 4-methoxybenzoate monooxygenase (O-demethylating) () is an enzyme that catalyzes the chemical reaction
4-methoxybenzoate + AH2 + O2 4-hydroxybenzoate + formaldehyde + A + H2O
The 3 substrates of this enzyme are 4-methoxybenzoate, an electron acceptor AH2, and O2, whereas its 4 products are 4-hydroxybenzoate, formaldehyde, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is 4-methoxybenzoate,hydrogen-donor:oxygen oxidoreductase (O-demethylating). Other names in common use include 4-methoxybenzoate 4-monooxygenase (O-demethylating), 4-methoxybenzoate O-demethylase, p-anisic O-demethylase, and piperonylate-4-O-demethylase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4%27-methoxyisoflavone%202%27-hydroxylase | In enzymology, a 4'-methoxyisoflavone 2'-hydroxylase (, Formerly ) is an enzyme that catalyzes the chemical reaction
formononetin + NADPH + H+ + O2 2'-hydroxyformononetin + NADP+ + H2O
The 4 substrates of this enzyme are formononetin, NADPH, H+, and O2, whereas its 3 products are 2'-hydroxyformononetin, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is formononetin,NADPH:oxygen oxidoreductase (2'-hydroxylating). Other names in common use include isoflavone 2'-monooxygenase (ambiguous), and isoflavone 2'-hydroxylase (ambiguous). This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.
References
EC 1.14.14
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/4-nitrophenol%202-monooxygenase | In enzymology, a 4-nitrophenol 2-monooxygenase () is an enzyme that catalyzes the chemical reaction
4-nitrophenol + NADH + H+ + O2 4-nitrocatechol + NAD+ + H2O
The 4 substrates of this enzyme are 4-nitrophenol, NADH, H+, and O2, whereas its 3 products are 4-nitrocatechol, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-nitrophenol,NADH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 4-nitrophenol hydroxylase, and 4-nitrophenol-2-hydroxylase. This enzyme participates in gamma-hexachlorocyclohexane degradation. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-sulfobenzoate%203%2C4-dioxygenase | In enzymology, a 4-sulfobenzoate 3,4-dioxygenase () is an enzyme that catalyzes the chemical reaction
4-sulfobenzoate + NADH + H+ + O2 3,4-dihydroxybenzoate + sulfite + NAD+
The 4 substrates of this enzyme are 4-sulfobenzoate, NADH, H+, and O2, whereas its 3 products are 3,4-dihydroxybenzoate, sulfite, and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 4-sulfobenzoate,NADH:oxygen oxidoreductase (3,4-hydroxylating, sulfite-forming). Other names in common use include 4-sulfobenzoate dioxygenase, and 4-sulfobenzoate 3,4-dioxygenase system. This enzyme participates in 2,4-dichlorobenzoate degradation. It has 3 cofactors: iron, FMN, and Iron-sulfur.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Iron enzymes
Flavoproteins
Iron-sulfur enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5beta-cholestane-3alpha%2C7alpha-diol%2012alpha-hydroxylase | In enzymology, a 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase () is an enzyme that catalyzes the chemical reaction
5beta-cholestane-3alpha,7alpha-diol + NADPH + H+ + O2 5beta-cholestane-3alpha,7alpha,12alpha-triol + NADP+ + H2O
The 4 substrates of this enzyme are 5beta-cholestane-3alpha,7alpha-diol, NADPH, H+, and O2, whereas its 3 products are 5beta-cholestane-3alpha,7alpha,12alpha-triol, NADP+, and H2O.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 5beta-cholestane-3alpha,7alpha-diol,NADPH:oxygen oxidoreductase (12alpha-hydroxylating). Other names in common use include 5beta-cholestane-3alpha,7alpha-diol 12alpha-monooxygenase, sterol 12alpha-hydroxylase (ambiguous), CYP8B1, and cytochrome P450 8B1.
References
Further reading
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-O-%284-coumaroyl%29-D-quinate%203%27-monooxygenase | In enzymology, a 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase () is an enzyme that catalyzes the chemical reaction
trans-5-O-(4-coumaroyl)-D-quinate + NADPH + H+ + O2 trans-5-O-caffeoyl-D-quinate + NADP+ + H2O
The 4 substrates of this enzyme are trans-5-O-(4-coumaroyl)-D-quinate, NADPH, H+, and O2, whereas its 3 products are trans-5-O-caffeoyl-D-quinate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is trans-5-O-(4-coumaroyl)-D-quinate,NADPH:oxygen oxidoreductase (3'-hydroxylating). Other names in common use include 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase, and coumaroylquinate(coumaroylshikimate) 3'-monooxygenase. This enzyme participates in phenylpropanoid biosynthesis.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/5-pyridoxate%20dioxygenase | In enzymology, a 5-pyridoxate dioxygenase () is an enzyme that catalyzes the chemical reaction
3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + H+ + O2 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+
The 4 substrates of this enzyme are 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate, NADPH, H+, and O2, whereas its two products are 2-(acetamidomethylene)-3-(hydroxymethyl)succinate and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 5-pyridoxate,NADPH:oxygen oxidoreductase (decyclizing). This enzyme is also called 5-pyridoxate oxidase. This enzyme participates in vitamin B6 metabolism. It has 2 cofactors: FAD, and Flavoprotein.
References
EC 1.14.12
NADPH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6%CE%B2-Hydroxyhyoscyamine%20epoxidase | In enzymology, a 6β-hydroxyhyoscyamine epoxidase () is an enzyme that catalyzes the chemical reaction
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2 scopolamine + succinate + CO2 + H2O
The 3 substrates of this enzyme are (6S)-6-hydroxyhyoscyamine, 2-oxoglutarate, and O2, whereas its 4 products are scopolamine, succinate, CO2, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor. This enzyme participates in alkaloid biosynthesis ii. It has two cofactors: iron and ascorbate.
Nomenclature
The systematic name of this enzyme class is (6S)-6-hydroxyhyoscyamine,2-oxoglutarate oxidoreductase (epoxide-forming). This enzyme is also called hydroxyhyoscyamine dioxygenase.
References
EC 1.14.11
Iron enzymes
Ascorbate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-oxocineole%20dehydrogenase | In enzymology, a 6-oxocineole dehydrogenase () is an enzyme that catalyzes the chemical reaction
6-oxocineole + NADPH + H+ + O2 1,6,6-trimethyl-2,7-dioxabicyclo[3.2.2]nonan-3-one + NADP+ + H2O
The 4 substrates of this enzyme are 6-oxocineole, NADPH, H+, and O2, whereas its 3 products are [[1,6,6-trimethyl-2,7-dioxabicyclo[3.2.2]nonan-3-one]], NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 6-oxocineole,NADPH:oxygen oxidoreductase. This enzyme is also called 6-oxocineole oxygenase. This enzyme participates in terpenoid biosynthesis.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/7alpha-hydroxycholest-4-en-3-one%2012alpha-hydroxylase | 7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase (, previously ) is an enzyme that catalyzes the chemical reaction:
7alpha-hydroxycholest-4-en-3-one + NADPH + H+ + O2 7alpha,12alpha-dihydroxycholest-4-en-3-one + NADP+ + H2O
The 4 substrates of this enzyme are 7alpha-hydroxycholest-4-en-3-one (7 alpha-hydroxy-4-cholesten-3-one, NADPH, H+, and O2. Its products are 7alpha,12alpha-dihydroxycholest-4-en-3-one, NADP+, and H2O.
Since 2015, the enzyme has been classified with with the systematic name of 5β-cholestan-3α,7α-diol 12α-hydroxylase. Other names that have been used include 7alpha-hydroxycholest-4-en-3-one,NADPH:oxygen oxidoreductase (12alpha-hydroxylating), 7alpha-hydroxy-4-cholesten-3-one 12alpha-monooxygenase, CYP12, sterol 12alpha-hydroxylase (ambiguous), and HCO 12alpha-hydroxylase.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2, with NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor. It was purified and characterized from rabbit liver microsomes in 1992 and was cloned and sequenced in 1996. Its structure was 39% similar to human prostacyclin synthase (CYP8) and 31% similar to cholesterol 7 alpha-hydroxylase (CYP7).
This enzymatic activity is now known to be performed by the product of the CYP8B1 gene. This step leads to the formation of the bile acid cholic |
https://en.wikipedia.org/wiki/7-deoxyloganin%207-hydroxylase | In enzymology, a 7-deoxyloganin 7-hydroxylase () is an enzyme that catalyzes the chemical reaction
7-deoxyloganin + NADPH + H+ + O2 loganin + NADP+ + H2O
The 4 substrates of this enzyme are 7-deoxyloganin, NADPH, H+, and O2, whereas its 3 products are loganin, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 7-deoxyloganin,NADPH:oxygen oxidoreductase (7alpha-hydroxylating). This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/8-dimethylallylnaringenin%202%27-hydroxylase | In enzymology, a 8-dimethylallylnaringenin 2'-hydroxylase () is an enzyme that catalyzes the chemical reaction
sophoraflavanone B + NADPH + H+ + O2 leachianone G + NADP+ + H2O
The 4 substrates of this enzyme are sophoraflavanone B, NADPH, H+, and O2, whereas its 3 products are leachianone G, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is sophoraflavanone-B,NADPH:oxygen oxidoreductase (2'-hydroxylating). This enzyme is also called 8-DMAN 2'-hydroxylase.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28%2B%29-abscisic%20acid%208%27-hydroxylase | In enzymology, a (+)-abscisic acid 8'-hydroxylase () is an enzyme that catalyzes the chemical reaction
(+)-abscisate + NADPH + H + O 8'-hydroxyabscisate + NADP + HO
The four substrates of this enzyme are (+)-abscisate, NADPH, H, and O, whereas its three products are 8'-hydroxy-abscisate, NADP, and HO.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on paired donors, with O as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O with NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor. This enzyme participates in carotenoid biosynthesis.
Nomenclature
The systematic name of this enzyme class is abscisate,NADPH:oxygen oxidoreductase (8'-hydroxylating). Other names in common use include
(+)-ABA 8'-hydroxylase and
ABA 8'-hydroxylase.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acyl-%28acyl-carrier-protein%29%20desaturase | In enzymology, an acyl-[acyl-carrier-protein] desaturase () is an enzyme that catalyzes the chemical reaction
stearoyl-[acyl-carrier-protein] + reduced acceptor + O2 oleoyl-[acyl-carrier-protein] + acceptor + 2 H2O
The systematic name of this enzyme class is acyl-[acyl-carrier-protein], hydrogen-donor:oxygen oxidoreductase. Other names in common use include stearyl acyl carrier protein desaturase, and stearyl-ACP desaturase. This enzyme participates in polyunsaturated fatty acid biosynthesis. It employs one cofactor, ferredoxin.
Reaction
The 3 substrates of this enzyme are stearoyl-(acyl-carrier-protein), reduced acceptor, and O2, whereas its 3 products are oleoyl-(acyl-carrier-protein), acceptor, and H2O.
The precise mechanism of this class of enzymes is not known, however recent studies using the kinetic isotope effect suggest that the rate limiting step is the removal of a hydrogen from the carbon nearest the carboxylic acid group. The diiron cluster moves through to a peroxo intermediate which can then dehydrate the short-lived alcohol intermediate, liberating water. There are a variety of specific enzymes within this class that attack using this mechanism, but do so at different points along the carbon chain of their respective fatty acids
Biological Function
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived fr |
https://en.wikipedia.org/wiki/Albendazole%20monooxygenase | In enzymology, an albendazole monooxygenase () is an enzyme that catalyzes the chemical reaction
albendazole + NADPH + H+ + O2 albendazole S-oxide + NADP+ + H2O
The four substrates of this enzyme are albendazole, NADPH, H+, and O2, whereas its three products are albendazole S-oxide, NADP+, and H2O.
This enzyme is coded by the gene for CYP3A4 and belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is albendazole,NADPH:oxygen oxidoreductase (sulfoxide-forming). Other names in common use include albendazole oxidase, and albendazole sulfoxidase. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkanal%20monooxygenase%20%28FMN-linked%29 | In enzymology, an alkanal monooxygenase (FMN-linked) () is an enzyme that catalyzes the chemical reaction
RCHO + reduced FMN + O2 RCOOH + FMN + H2O + hnu
The 3 substrates of this enzyme are RCHO, reduced FMN, and O2, whereas its 4 products are RCOOH, FMN, H2O, and hn.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is alkanal, reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing). Other names in common use include bacterial luciferase, aldehyde monooxygenase, luciferase, and Vibrio fischeri luciferase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.14.14
Enzymes of known structure |
https://en.wikipedia.org/wiki/Alkane%201-monooxygenase | In enzymology, an alkane 1-monooxygenase () is an enzyme that catalyzes the chemical reactions
an alkane + reduced rubredoxin + O2 a primary alcohol + oxidized rubredoxin + H2O.
Alkanes of 6 to 22 carbons have been observed as substrates. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with oxygen as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is alkane, reduced-rubredoxin:oxygen 1-oxidoreductase. Other names in common use include alkane 1-hydroxylase, omega-hydroxylase, fatty acid omega-hydroxylase, alkane monooxygenase, 1-hydroxylase, AlkB, and alkane hydroxylase. It contains a diiron non-heme active site.
Recently two crystal structures of the enzyme have appeared that provide much more information about the structure of the enzyme. Both structures show an unusual diiron active site where the two iron ions are separated by more than 5 angstroms. Neither structure shows evidence for a ligand that would bridge the two iron ions.
References
EC 1.14.15
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkanesulfonate%20monooxygenase | In enzymology, an alkanesulfonate monooxygenase () is an enzyme that catalyzes the chemical reaction
an alkanesulfonate (R-CH2-SO3H) + FMNH2 + O2 an aldehyde (R-CHO) + FMN + sulfite + H2O
The 3 substrates of this enzyme are alkanesulfonate (R-CH2-SO3H), FMNH2, and O2, whereas its 4 products are aldehyde, FMN, sulfite, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is alkanesulfonate, reduced-FMN:oxygen oxidoreductase. Other names in common use include SsuD, and sulfate starvation-induced protein 6.
References
External links
Xuanzhi Zhan, Russell A. Carpenter, and Holly R. Ellis, "Catalytic Importance of the Substrate Binding Order for the FMNH2-Dependent Alkanesulfonate Monooxygenase Enzyme", Biochemistry, 2008, 47 (7), pp. 2221–2230.
EC 1.14.14
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkene%20monooxygenase | In enzymology, an alkene monooxygenase () is an enzyme that catalyzes the chemical reaction
propene + NADH + H+ + O2 1,2-epoxypropane + NAD+ + H2O
The 4 substrates of this enzyme are propene, NADH, H+, and O2, whereas its 3 products are 1,2-epoxypropane, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is alkene,NADH:oxygen oxidoreductase. This enzyme is also called alkene epoxygenase. This enzyme participates in tetrachloroethene degradation.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aminocyclopropanecarboxylate%20oxidase | In enzymology, an aminocyclopropanecarboxylate oxidase () is an enzyme that catalyzes the chemical reaction
1-aminocyclopropane-1-carboxylate + ascorbate + O2 ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
The 3 substrates of this enzyme are 1-aminocyclopropane-1-carboxylate, ascorbate, and O2, whereas its 5 products are ethylene, cyanide, dehydroascorbate, CO2, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate oxygenase (ethylene-forming). Other names in common use include ACC oxidase, and ethylene-forming enzyme.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
Reaction Mechanism
Mechanistic and structural studies support binding of ACC and oxygen to an iron center located in the active site of ACC oxidase. The ring-opening of bound ACC is believed to result in the elimination of ethylene together with an unstable intermediate, cyanoformate ion, which then decomposes to cyanide ion and carbon dioxide. Cyanide ion is a known deactivating agent for iron-containing enzymes, but the cyanoformate ion intermediate is believed to play a vital role to |
https://en.wikipedia.org/wiki/Androst-4-ene-3%2C17-dione%20monooxygenase | In enzymology, an androst-4-ene-3,17-dione monooxygenase () is an enzyme that catalyzes the chemical reaction
androst-4-ene-3,17-dione + AH2 + O2 3-oxo-13,17-secoandrost-4-ene-17,13alpha-lactone + A + H2O
The 3 substrates of this enzyme are androst-4-ene-3,17-dione, an electron acceptor AH2, and O2, whereas its 3 products are 3-oxo-13,17-secoandrost-4-ene-17,13alpha-lactone, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is androst-4-ene-3,17-dione-hydrogen-donor:oxygen oxidorcockeductase (13-hydroxylating, lactonizing). Other names in common use include androstene-3,17-dione hydroxylase, androst-4-ene-3,17-dione 17-oxidoreductase, androst-4-ene-3,17-dione hydroxylase, androstenedione monooxygenase, and 4-androstene-3,17-dione monooxygenase. This enzyme participates in androgen and estrogen metabolism.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Anhydrotetracycline%20monooxygenase | In enzymology, an anhydrotetracycline monooxygenase () is an enzyme that catalyzes the chemical reaction
anhydrotetracycline + NADPH + H+ + O2 12-dehydrotetracycline + NADP+ + H2O
The 4 substrates of this enzyme are anhydrotetracycline, NADPH, H+, and O2, whereas its 3 products are 12-dehydrotetracycline, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is anhydrotetracycline,NADPH:oxygen oxidoreductase (6-hydroxylating). Other names in common use include ATC oxygenase, and anhydrotetracycline oxygenase. This enzyme participates in tetracycline biosynthesis and biosynthesis of type ii polyketide products.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Anthranilate%201%2C2-dioxygenase%20%28deaminating%2C%20decarboxylating%29 | In enzymology, an anthranilate 1,2-dioxygenase (deaminating, decarboxylating) () is an enzyme that catalyzes the chemical reaction
anthranilate + NAD(P)H + 2 H+ + O2 catechol + CO2 + NAD(P)+ + NH3
The 5 substrates of this enzyme are anthranilate, NADH, NADPH, H+, and O2, whereas its 5 products are catechol, CO2, NAD+, NADP+, and NH3.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is anthranilate,NAD(P)H:oxygen oxidoreductase (1,2-hydroxylating, deaminating, decarboxylating). Other names in common use include anthranilate hydroxylase, anthranilic hydroxylase, and anthranilic acid hydroxylase. This enzyme participates in 3 metabolic pathways: benzoate degradation via hydroxylation, carbazole degradation, and nitrogen metabolism. It employs one cofactor, iron.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Iron enzymes
Enzymes of unknown structure
Anthranilates |
https://en.wikipedia.org/wiki/Anthranilate%203-monooxygenase | In enzymology, an anthranilate 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
anthranilate + tetrahydrobiopterin + O2 3-hydroxyanthranilate + dihydrobiopterin + H2O
The 3 substrates of this enzyme are anthranilate, tetrahydrobiopterin, and O2, whereas its 3 products are 3-hydroxyanthranilate, dihydrobiopterin, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced pteridine as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is anthranilate,tetrahydrobiopterin:oxygen oxidoreductase (3-hydroxylating). Other names in common use include anthranilate 3-hydroxylase, anthranilate hydroxylase, anthranilic hydroxylase, and anthranilic acid hydroxylase. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron.
References
EC 1.14.16
Iron enzymes
Enzymes of unknown structure
Anthranilates |
https://en.wikipedia.org/wiki/Anthranilate%203-monooxygenase%20%28deaminating%29 | In enzymology, an anthranilate 3-monooxygenase (deaminating) () is an enzyme that catalyzes the chemical reaction
anthranilate + NADPH + H+ + O2 2,3-dihydroxybenzoate + NADP+ + NH3
The 4 substrates of this enzyme are anthranilate, NADPH, H+, and O2, whereas its 3 products are 2,3-dihydroxybenzoate, NADP+, and NH3.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is anthranilate,NADPH:oxygen oxidoreductase (3-hydroxylating, deaminating). Other names in common use include anthranilate hydroxylase, anthranilate 2,3-dioxygenase (deaminating), anthranilate hydroxylase (deaminating), anthranilic hydroxylase, and anthranilate 2,3-hydroxylase (deaminating). This enzyme participates in 3 metabolic pathways: benzoate degradation via hydroxylation, carbazole degradation, and nitrogen metabolism.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure
Anthranilates |
https://en.wikipedia.org/wiki/Anthraniloyl-CoA%20monooxygenase | In enzymology, an anthraniloyl-CoA monooxygenase () is an enzyme that catalyzes the chemical reaction
2-aminobenzoyl-CoA + 2 NAD(P)H + 2 H+ + O2 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
The 5 substrates of this enzyme are 2-aminobenzoyl-CoA, NADH, NADPH, H+, and O2, whereas its 4 products are 2-amino-5-oxocyclohex-1-enecarboxyl-CoA, H2O, NAD+, and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-aminobenzoyl-CoA,NAD(P)H:oxygen oxidoreductase (de-aromatizing). Other names in common use include anthraniloyl coenzyme A reductase, and 2-aminobenzoyl-CoA monooxygenase/reductase. This enzyme participates in carbazole degradation. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Benzene%201%2C2-dioxygenase | In enzymology, a benzene 1,2-dioxygenase () is an enzyme that catalyzes the chemical reaction
benzene + NADH + H+ + O2 cis-cyclohexa-3,5-diene-1,2-diol + NAD+
The 4 substrates of this enzyme are benzene, NADH, H+, and O2, whereas its two products are cis-cyclohexa-3,5-diene-1,2-diol and NAD+.
Classification
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor.
Nomenclature
The systematic name of this enzyme class is benzene,NADH:oxygen oxidoreductase (1,2-hydroxylating). Other names in common use include benzene hydroxylase, and benzene dioxygenase.
Biological role
This enzyme participates in naphthalene and anthracene degradation. It has 4 cofactors: FAD, Iron, Sulfur, and Iron-sulfur.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Iron enzymes
Sulfur enzymes
Iron-sulfur enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Benzoate%201%2C2-dioxygenase | In enzymology, a benzoate 1,2-dioxygenase () is an enzyme that catalyzes the chemical reaction
benzoate + NADH + H+ + O2 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
The 4 substrates of this enzyme are benzoate, NADH, H+, and O2, whereas its two products are 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is benzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating). Other names in common use include benzoate hydroxylase, benzoate hydroxylase, benzoic hydroxylase, benzoate dioxygenase, benzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating,, and decarboxylating) [incorrect]. This enzyme participates in benzoate degradation via hydroxylation and benzoate degradation via coa ligation. It has 3 cofactors: FAD, Iron, and Sulfur.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Iron enzymes
Sulfur enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Benzoate%204-monooxygenase | In enzymology, a benzoate 4-monooxygenase (, Formerly ) is an enzyme that catalyzes the chemical reaction
benzoate + NADPH + H+ + O2 4-hydroxybenzoate + NADP+ + H2O
The 4 substrates of this enzyme are benzoate, NADPH, H+, and O2, whereas its 3 products are 4-hydroxybenzoate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is benzoate,NADPH:oxygen oxidoreductase (4-hydroxylating). Other names in common use include benzoic acid 4-hydroxylase, benzoate 4-hydroxylase, benzoic 4-hydroxylase, benzoate-p-hydroxylase, and p-hydroxybenzoate hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and benzoate degradation via coa ligation. It has 3 cofactors: iron, Tetrahydrobiopterin, and Tetrahydropteridine.
References
EC 1.14.14
NADPH-dependent enzymes
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Benzoyl-CoA%203-monooxygenase | In enzymology, a benzoyl-CoA 3-monooxygenase () is an enzyme that catalyzes the chemical reaction:
benzoyl-CoA + NADPH + H+ + O2 3-hydroxybenzoyl-CoA + NADP+ + H2O
The 4 substrates of this enzyme are benzoyl-CoA, NADPH, H+, and O2, whereas its 3 products are 3-hydroxybenzoyl-CoA, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is benzoyl-CoA,NADPH:oxygen oxidoreductase (3-hydroxylating). This enzyme is also called benzoyl-CoA 3-hydroxylase.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Berbamunine%20synthase | In enzymology, a berbamunine synthase (, Formerly and ) is an enzyme that catalyzes the chemical reaction
(S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + H+ + O2 berbamunine + NADP+ + 2 H2O
The 5 substrates of this enzyme are (S)-N-methylcoclaurine, (R)-N-methylcoclaurine, NADPH, H+, and O2, whereas its 3 products are berbamunine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and the other dehydrogenated. The systematic name of this enzyme class is (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (C-O phenol-coupling). This enzyme is also called (S)-N-methylcoclaurine oxidase (C-O phenol-coupling). This enzyme participates in alkaloid biosynthesis i.
References
EC 1.14.19
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-carotene%2015%2C15%27-dioxygenase | In enzymology, beta-carotene 15,15'-dioxygenase, () is an enzyme with systematic name beta-carotene:oxygen 15,15'-dioxygenase (bond-cleaving). In human it is encoded by the BCDO2 gene. This enzyme catalyses the following chemical reaction
beta-carotene + O2 → 2 all-trans-retinal
This is a cleavage reaction which cleaves β-carotene, utilizes molecular oxygen, is enhanced by the presence of bile salts and thyroxine, and generates two molecules of retinal. In humans, the enzyme is present in the small intestine and liver. The dioxygenase also asymmetrically cleaves beta-cryptoxanthin, trans-β-apo-8'-carotenal, beta-4'-apo-β-carotenal, alpha-carotene and gamma-carotene in decreasing order, creating one retinal molecule, all of these being substrates with a carbon chain greater than C30, with at least one unsubstituted β-ionone ring.
This enzyme belongs to the (enzymatically-defined) family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. A related enzyme is β-carotene 15,15'-monooxygenase, coded for by the gene BCMO1, which symmetrically cleaves β-carotene into two retinal molecules.
In general, carnivores are poor converters of ionone-containing carotenoids, and pure carnivores such as felids (cats) lack beta-carotene 15,15'-dioxygenase and beta-carotene 15,15'-monooxygenase and cannot convert any carotenoids to retinal, resulting in none of the carotenoids being forms of vitamin A for these species |
https://en.wikipedia.org/wiki/Biphenyl%202%2C3-dioxygenase | In enzymology, a biphenyl 2,3-dioxygenase () is an enzyme that catalyzes the chemical reaction
biphenyl + NADH + H+ + O2 (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
The 4 substrates of this enzyme are biphenyl, NADH, H+, and O2, whereas its two products are (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is biphenyl,NADH:oxygen oxidoreductase (2,3-hydroxylating). This enzyme is also called biphenyl dioxygenase. This enzyme participates in biphenyl degradation.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Camphor%201%2C2-monooxygenase | In enzymology, a camphor 1,2-monooxygenase () is an enzyme that catalyzes the chemical reaction
(+)-bornane-2,5-dione + reduced rubredoxin + O2 5-oxo-1,2-campholide + oxidized rubredoxin + H2O
The 3 substrates of this enzyme are (+)-bornane-2,5-dione, reduced rubredoxin, and O2, whereas its 3 products are 5-oxo-1,2-campholide, oxidized rubredoxin, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation o one atom of oxygen into the other donor. The systematic name of this enzyme class is (+)-camphor,reduced-rubredoxin:oxygen oxidoreductase (1,2-lactonizing). Other names in common use include 2,5-diketocamphane lactonizing enzyme, camphor ketolactonase I, oxygenase, camphor 1,2-mono, and ketolactonase I. It employs one cofactor, iron.
References
EC 1.14.15
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Camphor%205-monooxygenase | In enzymology, a camphor 5-monooxygenase () is an enzyme that catalyzes the chemical reaction
(+)-camphor + putidaredoxin + O2 (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
The 3 substrates of this enzyme are (+)-camphor, putidaredoxin, and O2, whereas its 3 products are (+)-exo-5-hydroxycamphor, oxidized putidaredoxin, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is (+)-camphor,reduced putidaredoxin:oxygen oxidoreductase (5-hydroxylating). Other names in common use include camphor 5-exo-methylene hydroxylase, 2-bornanone 5-exo-hydroxylase, bornanone 5-exo-hydroxylase, camphor 5-exo-hydroxylase, camphor 5-exohydroxylase, camphor hydroxylase, d-camphor monooxygenase, methylene hydroxylase, methylene monooxygenase, D-camphor-exo-hydroxylase, and camphor methylene hydroxylase. It employs one cofactor, heme.
Structural studies
As of late 2007, 58 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
Examples
Cytochrome P450 camphor 5-monooxygenase is a bacterial enzyme originally from Pseudomonas pu |
https://en.wikipedia.org/wiki/Carotene%207%2C8-desaturase | In enzymology, a carotene 7,8-desaturase () is an enzyme that catalyzes the chemical reaction
neurosporene + AH2 + O2 lycopene + A + 2 H2O
The 3 substrates of this enzyme are neurosporene, an electron acceptor AH2, and O2, whereas its 3 products are lycopene, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O miscellaneous. The systematic name of this enzyme class is carotene, hydrogen-donor:oxygen oxidoreductase. This enzyme is also called zeta-carotene desaturase. This enzyme participates in carotenoid biosynthesis - general.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cholestanetriol%2026-monooxygenase | In enzymology, a cholestanetriol 26-monooxygenase () is an enzyme that catalyzes the chemical reaction
5beta-cholestane-3alpha,7alpha,12alpha-triol + NADPH + H+ + O2 (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NADP+ + H2O
The 4 substrates of this enzyme are 5beta-cholestane-3alpha,7alpha,12alpha-triol, NADPH, H+, and O2, whereas its 3 products are (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 5beta-cholestane-3alpha,7alpha,12alpha-triol,NADPH:oxygen oxidoreductase (26-hydroxylating). Other names in common use include 5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase, 5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase, cholestanetriol 26-hydroxylase, sterol 27-hydroxylase, sterol 26-hydroxylase, cholesterol 27-hydroxylase, CYP27A, CYP27A1, and cytochrome P450 27A1'. This enzyme participates in bile acid biosynthesis and ppar signaling pathway.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cholesterol%2024-hydroxylase | Cholesterol 24-hydroxylase (), also commonly known as cholesterol 24S-hydroxylase, cholesterol 24-monooxygenase, CYP46, or CYP46A1, is an enzyme that catalyzes the conversion of cholesterol to 24S-hydroxycholesterol. It is responsible for the majority of cholesterol turnover in the human central nervous system. The systematic name of this enzyme class is cholesterol,NADPH:oxygen oxidoreductase (24-hydroxylating).
This enzyme is a member of the cytochrome P450 (CYP) superfamily of enzymes. Like many other CYP enzymes that act on cholesterol, cholesterol-24 hydroxylase is a monooxygenase that hydroxylates the side-chain of cholesterol.
Because 24S-hydroxycholesterol is more polar than cholesterol, it can more easily pass the blood–brain barrier to exit the brain and pass into the bloodstream, where it can then travel to the liver to be further degraded. This enzyme has also been found at low quantities in the retina, where it performs the same function to a lesser degree.
Genetic cloning of the encoding gene (CYP46A1) was first accomplished in 1999 and an extensive E. coli expression and purification system was later developed in 2003.
Molecular structure
The enzymatic structure of the human cholesterol-24 hydroxylase was determined via crystallography at the Stanford Synchrotron Radiation Lightsource, and was shown to be a 57kDa (500 residue) monomeric heme-containing protein bound to the endoplasmic reticulum in neurons.
Cholesterol-24 hydroxylase is similar in structure |
https://en.wikipedia.org/wiki/Cholesterol%2025-hydroxylase | In enzymology, a cholesterol 25-hydroxylase () is an enzyme that catalyzes the chemical reaction
cholesterol + AH2 + O2 25-hydroxycholesterol + A + H2O
The 3 substrates of this enzyme are cholesterol, an electron acceptor AH2, and O2, whereas its 3 products are 25-hydroxycholesterol (25HC), the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is cholesterol, hydrogen-donor:oxygen oxidoreductase (25-hydroxylating). This enzyme is also called cholesterol 25-monooxygenase.
Transcripts for this enzyme have been identified in macrophages from the testis.
CH25H is an interferon-stimulated gene, and its primary product 25HC may have broad-spectrum antiviral activity, demonstrated in mice against HIV, ebola, Nipah virus, Rift Valley Fever virus, and SARS-CoV-2. Specifically, 25HC blocks membrane fusion between the cell and virus, and may "implicate membrane-modifying oxysterols as potential antiviral therapeutics.” Recently, upregulation of CH25H has been shown to play a role in effectively restricting infection of lung epithelial cells with SARS-Cov-2 through its enzymatic product, 25HC, which depletes accessible membrane cholesterol so that the virus is unable to achieve fusion with the cell membrane necessary for entry and infection |
https://en.wikipedia.org/wiki/Cholesterol%207alpha-monooxygenase | In enzymology, a cholesterol 7alpha-monooxygenase () is an enzyme that catalyzes the chemical reaction
cholesterol + NADPH + H+ + O2 7alpha-hydroxycholesterol + NADP+ + H2O
The 4 substrates of this enzyme are cholesterol, NADPH, H+, and O2, whereas its 3 products are 7-alpha-hydroxycholesterol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is cholesterol,NADPH:oxygen oxidoreductase (7alpha-hydroxylating). Other names in common use include cholesterol 7alpha-hydroxylase, and CYP7A1. This enzyme participates in bile acid biosynthesis and ppar signaling pathway. It employs one cofactor, heme.
References
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Choline%20monooxygenase | In enzymology, a choline monooxygenase () is an enzyme that catalyzes the chemical reaction
choline + O2 + 2 reduced ferredoxin + 2 H+ betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
The 4 substrates of this enzyme are choline, O2, reduced ferredoxin, and H+, whereas its 3 products are betaine aldehyde hydrate, H2O, and oxidized ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation o one atom of oxygen into the other donor. The systematic name of this enzyme class is choline, reduced-ferredoxin:oxygen oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism.
References
EC 1.14.15
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CMP-N-acetylneuraminate%20monooxygenase | In enzymology, a CMP-N-acetylneuraminate monooxygenase () is an enzyme that catalyzes the chemical reaction
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+ CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
The 4 substrates of this enzyme are CMP-N-acetylneuraminate, ferrocytochrome b5, O2, and H+, whereas its 3 products are CMP-N-glycoloylneuraminate, ferricytochrome b5, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with another compound as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is CMP-N-acetylneuraminate,ferrocytochrome-b5:oxygen oxidoreductase (N-acetyl-hydroxylating). Other names in common use include CMP-N-acetylneuraminic acid hydroxylase, CMP-Neu5Ac hydroxylase, cytidine monophosphoacetylneuraminate monooxygenase, N-acetylneuraminic monooxygenase, and cytidine-5'-monophosphate-N-acetylneuraminic acid hydroxylase. This enzyme participates in aminosugars metabolism.
References
EC 1.14.18
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Corticosterone%2018-monooxygenase | In enzymology, a corticosterone 18-monooxygenase () is an enzyme that catalyzes the chemical reaction
corticosterone + reduced adrenal ferredoxin + O2 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
The 3 substrates of this enzyme are corticosterone, reduced adrenal ferredoxin, and O2, whereas its 3 products are 18-hydroxycorticosterone, oxidized adrenal ferredoxin, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is corticosterone,reduced-adrenal-ferredoxin:oxygen oxidoreductase (18-hydroxylating). Other names in common use include corticosterone 18-hydroxylase, and corticosterone methyl oxidase. This enzyme participates in c21-steroid hormone metabolism.
References
EC 1.14.15
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclopentanone%20monooxygenase | In enzymology, a cyclopentanone monooxygenase () is an enzyme that catalyzes the chemical reaction
cyclopentanone + NADPH + H+ + O2 5-valerolactone + NADP+ + H2O
The 4 substrates of this enzyme are cyclopentanone, NADPH, H+, and O2, whereas its 3 products are 5-valerolactone, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is cyclopentanone,NADPH:oxygen oxidoreductase (5-hydroxylating, lactonizing). This enzyme is also called cyclopentanone oxygenase.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deacetoxycephalosporin-C%20hydroxylase | In enzymology, a deacetoxycephalosporin-C hydroxylase () is an enzyme that catalyzes the chemical reaction
deacetoxycephalosporin C + 2-oxoglutarate + O2 deacetylcephalosporin C + succinate + CO2
The 3 substrates of this enzyme are deacetoxycephalosporin C, 2-oxoglutarate, and O2, whereas its 3 products are deacetylcephalosporin C, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is deacetoxycephalosporin-C,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include deacetylcephalosporin C synthase, 3'-methylcephem hydroxylase, DACS, DAOC hydroxylase, and deacetoxycephalosporin C hydroxylase. This enzyme participates in penicillin and cephalosporin biosynthesis.
References
EC 1.14.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deacetoxycephalosporin-C%20synthase | In enzymology, a deacetoxycephalosporin-C synthase () is an enzyme that catalyzes the chemical reaction
penicillin N + 2-oxoglutarate + O2 deacetoxycephalosporin C + succinate + CO2 + H2O
The 3 substrates of this enzyme are penicillin N, 2-oxoglutarate, and O2, whereas its 4 products are deacetoxycephalosporin C, succinate, CO2, and H2O.
Classification
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and the other dehydrogenated.
Nomenclature
The systematic name of this enzyme class is penicillin-N,2-oxoglutarate:oxygen oxidoreductase (ring-expanding). Other names in common use include DAOCS, penicillin N expandase, and DAOC synthase.
Biological role
This enzyme participates in penicillin and cephalosporin biosynthesis.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 1.14.20
Enzymes of known structure |
https://en.wikipedia.org/wiki/Desacetoxyvindoline%204-hydroxylase | In enzymology, a desacetoxyvindoline 4-hydroxylase () is an enzyme that catalyzes the chemical reaction
desacetoxyvindoline + 2-oxoglutarate + O2 deacetylvindoline + succinate + CO2
The 3 substrates of this enzyme are desacetoxyvindoline, 2-oxoglutarate, and O2, whereas its 3 products are deacetylvindoline, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4beta-hydroxylating). Other names in common use include desacetoxyvindoline 4-hydroxylase, desacetyoxyvindoline-17-hydroxylase, D17H, desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase, and (4beta-hydroxylating). This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.
References
EC 1.14.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Delta12-fatty%20acid%20dehydrogenase | In enzymology, a Delta12-fatty acid dehydrogenase () is an enzyme that catalyzes the chemical reaction
linoleate + 2AH + O2 crepenynate + 2A + H2O
where AH is either NADH or NADPH.
The 3 substrates of this enzyme are linoleate, 2AH, and O2, whereas its 3 products are crepenynate, 2A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous.
This enzyme participates in linoleic acid metabolism.
Nomenclature
The systematic name of this enzyme class is linoleate, hydrogen-donor:oxygen oxidoreductase (Delta12-unsaturating). Other names in common use include
crepenynate synthase and
linoleate Delta12-fatty acid acetylenase (desaturase).
References
Further reading
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deoxyhypusine%20monooxygenase | In enzymology, a deoxyhypusine monooxygenase () is an enzyme that catalyzes the chemical reaction
protein N6-(4-aminobutyl)-L-lysine + AH2 + O2 protein N6-[(R)-4-amino-2-hydroxybutyl]-L-lysine + A + H2O
The 3 substrates of this enzyme are a protein-bound N6-(4-aminobutyl)-L-lysine, an electron acceptor AH2, and O2, and its 3 products are protein-bound N6-[(R)-4-amino-2-hydroxybutyl]-L-lysine, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is deoxyhypusine,hydrogen-donor:oxygen oxidoreductase (2-hydroxylating). Other names in common use include deoxyhypusine hydroxylase, and deoxyhypusine dioxygenase.
Mammalian proteins
The HUGO symbol for human gene and protein is DOHH, the full name is deoxyhypusine hydroxylase, and there are orthologs in other mammals. The orthologs have the same symbol, except for rodents, there the symbol is Dohh. The difference in case is just a meaningless historical artifact.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deoxysarpagine%20hydroxylase | In enzymology, a deoxysarpagine hydroxylase () is an enzyme that catalyzes the chemical reaction
10-deoxysarpagine + NADPH + H+ + O2 sarpagine + NADP+ + H2O
The 4 substrates of this enzyme are 10-deoxysarpagine, NADPH, H+, and O2, whereas its 3 products are sarpagine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 10-deoxysarpagine,NADPH:oxygen oxidoreductase (10-hydroxylating). This enzyme is also called DOSH.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrochelirubine%2012-monooxygenase | In enzymology, a dihydrochelirubine 12-monooxygenase () is an enzyme that catalyzes the chemical reaction
dihydrochelirubine + NADPH + H+ + O2 12-hydroxydihydrochelirubine + NADP+ + H2O
The 4 substrates of this enzyme are dihydrochelirubine, NADPH, H+, and O2, whereas its 3 products are 12-hydroxydihydrochelirubine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is dihydrochelirubine,NADPH:oxygen oxidoreductase (12-hydroxylating). This enzyme is also called dihydrochelirubine 12-hydroxylase. This enzyme participates in alkaloid biosynthesis i.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrosanguinarine%2010-monooxygenase | In enzymology, a dihydrosanguinarine 10-monooxygenase () is an enzyme that catalyzes the chemical reaction
dihydrosanguinarine + NADPH + H+ + O2 10-hydroxydihydrosanguinarine + NADP+ + H2O
The 4 substrates of this enzyme are dihydrosanguinarine, NADPH, H+, and O2, whereas its 3 products are 10-hydroxydihydrosanguinarine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is dihydrosanguinarine,NADPH:oxygen oxidoreductase (10-hydroxylating). This enzyme is also called dihydrosanguinarine 10-hydroxylase. This enzyme participates in alkaloid biosynthesis i.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dopamine%20beta-hydroxylase | Dopamine beta-hydroxylase (DBH), also known as dopamine beta-monooxygenase, is an enzyme () that in humans is encoded by the DBH gene. Dopamine beta-hydroxylase catalyzes the conversion of dopamine to norepinephrine.
The three substrates of the enzyme are dopamine, vitamin C (ascorbate), and O2. The products are norepinephrine, dehydroascorbate, and H2O.
DBH is a 290 kDa copper-containing oxygenase consisting of four identical subunits, and its activity requires ascorbate as a cofactor.
It is the only enzyme involved in the synthesis of small-molecule neurotransmitters that is membrane-bound, making norepinephrine the only known transmitter synthesized inside vesicles. It is expressed in noradrenergic neurons of the central nervous system (i.e. locus coeruleus) and peripheral nervous systems (i.e. sympathetic ganglia), as well as in chromaffin cells of the adrenal medulla.
Mechanism of catalysis
Based on the observations of what happens when there is no substrate, or oxygen, the following steps seem to constitute the hydroxylation reaction.
Although details of DBH mechanism are yet to be confirmed, DBH is homologous to another enzyme, peptidylglycine α-hydroxylating monooxygenase (PHM). Because DBH and PHM share similar structures, it is possible to model DBH mechanism based on what is known about PHM mechanism.
Substrate specificity
Dopamine beta-hydroxylase catalyzes the hydroxylation of not only dopamine but also other phenylethylamine derivatives when available |
https://en.wikipedia.org/wiki/Ecdysone%2020-monooxygenase | Ecdysone 20-monooxygenase () is an enzyme that catalyzes the chemical reaction
ecdysone + AH2 + O2 20-hydroxyecdysone + A + H2O
The three substrates of this enzyme are ecdysone, an electron acceptor AH2, and O2, whereas its three products are 20-hydroxyecdysone, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is ecdysone,hydrogen-donor:oxygen oxidoreductase (20-hydroxylating). Like other genes in the ecdysone synthesis pathway, it belongs to Cytochrome P450 Halloween genes, with the nickname shade, other names in common use include alpha-ecdysone C-20 hydroxylase, and ecdysone 20-hydroxylase.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Estradiol%206beta-monooxygenase | In enzymology, an estradiol 6beta-monooxygenase () is an enzyme that catalyzes the chemical reaction
estradiol-17beta + AH2 + O2 6beta-hydroxyestradiol-17beta + A + H2O
The 3 substrates of this enzyme are estradiol-17beta, an electron acceptor AH2, and O2, whereas its 3 products are 6beta-hydroxyestradiol-17beta, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is estradiol-17beta,hydrogen-donor:oxygen oxidoreductase (6beta-hydroxylating). This enzyme is also called estradiol 6beta-hydroxylase. This enzyme participates in androgen and estrogen metabolism.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Flavanone%203-dioxygenase | In enzymology, a flavanone 3-dioxygenase () is an enzyme that catalyzes the chemical reaction
a flavanone + 2-oxoglutarate + O2 a dihydroflavonol + succinate + CO2
The 3 substrates of this enzyme are flavanone, 2-oxoglutarate, and O2, whereas its 3 products are dihydroflavonol, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is flavanone,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include naringenin 3-hydroxylase, flavanone 3-hydroxylase, flavanone 3beta-hydroxylase, flavanone synthase I, (2S)-flavanone 3-hydroxylase, and naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme participates in flavonoid biosynthesis. It has 2 cofactors: iron, and Ascorbate.
References
EC 1.14.11
Iron enzymes
Ascorbate enzymes
Enzymes of unknown structure
Flavanones metabolism |
https://en.wikipedia.org/wiki/Flavone%20synthase | In enzymology, a flavone synthase () is an enzyme that catalyzes the chemical reaction
a flavanone + 2-oxoglutarate + O2 a flavone + succinate + CO2 + H2O
The 3 substrates of this enzyme are flavanone, 2-oxoglutarate, and O2, whereas its 4 products are flavone, succinate, CO2, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is flavanone,2-oxoglutarate:oxygen oxidoreductase (dehydrating). This enzyme participates in flavonoid biosynthesis and isoflavonoid biosynthesis.
References
EC 1.14.11
Enzymes of unknown structure
Flavones metabolism |
https://en.wikipedia.org/wiki/Flavonoid%203%27-monooxygenase | In enzymology, a flavonoid 3'-monooxygenase (, was wrongly classified as in the past) is an enzyme that catalyzes the chemical reaction
a flavonoid + NADPH + H+ + O2 a 3'-hydroxyflavonoid + NADP+ + H2O
The 4 substrates of this enzyme are flavonoid, NADPH, H+, and O2, whereas its 3 products are 3'-hydroxyflavonoid, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is flavonoid,NADPH:oxygen oxidoreductase (3'-hydroxylating). Other names in common use include flavonoid 3'-hydroxylase, flavonoid 3-hydroxylase (erroneous), NADPH:flavonoid-3'-hydroxylase, and flavonoid 3-monooxygenase (erroneous). This enzyme participates in flavonoid biosynthesis.
References
EC 1.14.14
NADPH-dependent enzymes
Enzymes of unknown structure
Flavonoids metabolism |
https://en.wikipedia.org/wiki/Flavonol%20synthase | In enzymology, a flavonol synthase () is an enzyme that catalyzes the following chemical reaction :
dihydroflavonol + 2-oxoglutarate + a flavonol + succinate + C + H2O
The 3 substrates of this enzyme are dihydroflavonol, 2-oxoglutarate, and O2, whereas its 4 products are flavonol, succinate, CO2, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from with 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor. The systematic name of this enzyme class is dihydroflavonol,2-oxoglutarate:oxygen oxidoreductase. This enzyme participates in flavonoid biosynthesis.
References
EC 1.14.11
Enzymes of unknown structure
Flavonols metabolism |
https://en.wikipedia.org/wiki/Gamma-butyrobetaine%20dioxygenase | Gamma-butyrobetaine dioxygenase (also known as BBOX, GBBH or γ-butyrobetaine hydroxylase) is an enzyme that in humans is encoded by the BBOX1 gene. Gamma-butyrobetaine dioxygenase catalyses the formation of L-carnitine from gamma-butyrobetaine, the last step in the L-carnitine biosynthesis pathway. Carnitine is essential for the transport of activated fatty acids across the mitochondrial membrane during mitochondrial beta oxidation. In humans, gamma-butyrobetaine dioxygenase can be found in the kidney (high), liver (moderate), and brain (very low). BBOX1 has recently been identified as a potential cancer gene based on a large-scale microarray data analysis.
Reaction
Gamma-butyrobetaine dioxygenase belongs to the 2-oxoglutarate (2OG)-dependent dioxygenase superfamily. It catalyses the following reaction:
4-trimethylammoniobutanoate (γ-butyrobetaine) + 2-oxoglutarate + O2 3-hydroxy-4-trimethylammoniobutanoate (L-carnitine) + succinate + CO2
The three substrates of this enzyme are 4-trimethylammoniobutanoate (γ-butyrobetaine), 2-oxoglutarate, and O2, whereas its three products are 3-hydroxy-4-trimethylammoniobutanoate (L-carnitine), succinate, and carbon dioxide.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor. This enzyme pa |
https://en.wikipedia.org/wiki/Gibberellin%202beta-dioxygenase | In enzymology, a gibberellin 2beta-dioxygenase () is an enzyme that catalyzes the chemical reaction
gibberellin 1 + 2-oxoglutarate + O2 2beta-hydroxygibberellin 1 + succinate + CO2
The 3 substrates of this enzyme are gibberellin 1, 2-oxoglutarate, and O2, whereas its 3 products are 2beta-hydroxygibberellin 1, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is (gibberellin-1),2-oxoglutarate:oxygen oxidoreductase (2beta-hydroxylating). This enzyme is also called gibberellin 2beta-hydroxylase. This enzyme participates in diterpenoid biosynthesis.
References
EC 1.14.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gibberellin%203beta-dioxygenase | In enzymology, a gibberellin 3beta-dioxygenase () is an enzyme that catalyzes the chemical reaction
gibberellin 20 + 2-oxoglutarate + O2 gibberellin 1 + succinate + CO2
The 3 substrates of this enzyme are gibberellin 20, 2-oxoglutarate, and O2, whereas its 3 products are gibberellin 1, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as the oxidant. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and one atom of oxygen is incorporated into each donor. The systematic name of this enzyme class is (gibberellin-20), 2-oxoglutarate: oxygen oxidoreductase (3beta-hydroxylating). Other names in common use include gibberellin 3beta-hydroxylase, (gibberrellin-20), 2-oxoglutarate: oxygen oxidoreductase and (3beta-hydroxylating). This enzyme participates in diterpenoid biosynthesis. It has 2 cofactors: iron and Ascorbate.
References
EC 1.14.11
Iron enzymes
Ascorbate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gibberellin-44%20dioxygenase | In enzymology, a gibberellin-44 dioxygenase () is an enzyme that catalyzes the chemical reaction
gibberellin 44 + 2-oxoglutarate + O2 gibberellin 19 + succinate + CO2
The 3 substrates of this enzyme are gibberellin 44, 2-oxoglutarate, and O2, whereas its 3 products are gibberellin 19, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is (gibberellin-44),2-oxoglutarate:oxygen oxidoreductase. Other names in common use include oxygenase, gibberellin A44 oxidase, and (gibberellin-44), 2-oxoglutarate:oxygen oxidoreductase. This enzyme participates in diterpenoid biosynthesis. It employs one cofactor, iron.
References
EC 1.14.11
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glyceollin%20synthase | In enzymology, a glyceollin synthase is an enzyme that catalyzes the last committed step in glyceollin biosynthesis. This enzyme has been classified as a cytochrome dependent monooxygenase. It uses cyclization of prenyl residue to convert glyceollidins (I and II) into glyceollins (I - III).
This enzyme catalyzes the following chemical reaction:
2-(or 4-)dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADPH + H+ + O2 glyceollin + NADP+ + 2 H2O
The five substrates of this enzyme are 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan, 4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan, NADPH, H+, and O2, whereas its three products are glyceollin, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-(or 4-)dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan,NADPH:oxygen oxidoreductase (cyclizing). This enzyme participates in isoflavonoid biosynthesis.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/Alkylglycerol%20monooxygenase | Alkylglycerol monooxygenase (AGMO) () is an enzyme that catalyzes the hydroxylation of alkylglycerols, a specific subclass of ether lipids. This enzyme was first described in 1964 as a pteridine-dependent ether lipid cleaving enzyme. In 2010 finally, the gene coding for alkylglycerol monooxygenase was discovered as transmembrane protein 195 (TMEM195) on chromosome 7.
In analogy to the enzymes phenylalanine hydroxylase, tyrosine hydroxylase, tryptophan hydroxylase and nitric oxide synthase, alkylglycerol monooxygenase critically depends on the cofactor tetrahydrobiopterin and iron.
The reaction catalyzed by alkylglycerol monooxygenase:
1-alkyl-sn-glycerol + tetrahydrobiopterin + O2 1-hydroxyalkyl-sn-glycerol + 6,7[8H]-dihydrobiopterin + H2O
The unstable intermediate product 1-hydroxyalkyl-sn-glycerol rearranges into the fatty aldehyde and the free glycerol derivative. The fatty aldehyde is then further oxidized to the corresponding acid by fatty aldehyde dehydrogenase.
Alkylglycerol monooxygenase is a membrane-bound mixed-function oxidase and harbours a fatty acid hydroxylase motif. The iron is believed to be coordinated by a diiron center composed of eight histidines, which can be found in all enzymes containing this motif.
Nomenclature
The systematic name for this enzyme is 1-alkyl-sn-glycerol,tetrahydrobiopterin:oxygen oxidoreductase. Other names in use are glyceryl-ether monooxygenase, glyceryl-ether cleaving enzyme, glyceryl ether oxygenase, glyceryl etherase, a |
https://en.wikipedia.org/wiki/Hydroxyphenylacetonitrile%202-monooxygenase | In enzymology, a hydroxyphenylacetonitrile 2-monooxygenase () is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylacetonitrile + NADPH + H+ + O2 4-hydroxymandelonitrile + NADP+ + H2O
The 4 substrates of this enzyme are 4-hydroxyphenylacetonitrile, NADPH, H+, and O2, whereas its 3 products are 4-hydroxymandelonitrile, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-hydroxyphenylacetonitrile,NADPH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 4-hydroxyphenylacetonitrile monooxygenase, and 4-hydroxyphenylacetonitrile hydroxylase. It employs one cofactor, heme.
References
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hyoscyamine%20%286S%29-dioxygenase | In enzymology, a hyoscyamine (6S)-dioxygenase () is an enzyme that catalyzes the chemical reaction
L-hyoscyamine + 2-oxoglutarate + O2 (6S)-hydroxyhyoscyamine + succinate + CO2
The 3 substrates of this enzyme are L-hyoscyamine, 2-oxoglutarate, and O2, whereas its 3 products are (6S)-hydroxyhyoscyamine, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is L-hyoscyamine,2-oxoglutarate:oxygen oxidoreductase ((6S)-hydroxylating). Other names in common use include hyoscyamine 6beta-hydroxylase, hyoscyamine 6beta-dioxygenase, and hyoscyamine 6-hydroxylase. This enzyme participates in alkaloid biosynthesis ii. It has 2 cofactors: iron, and Ascorbate.
References
EC 1.14.11
Iron enzymes
Ascorbate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Imidazoleacetate%204-monooxygenase | In enzymology, an imidazoleacetate 4-monooxygenase () is an enzyme that catalyzes the chemical reaction
4-imidazoleacetate + NADH + H+ + O2 5-hydroxy-4-imidazoleacetate + NAD+ + H2O
The 4 substrates of this enzyme are 4-imidazoleacetate, NADH, H+, and O2, whereas its 3 products are 5-hydroxy-4-imidazoleacetate, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-imidazoleacetate,NADH:oxygen oxidoreductase (5-hydroxylating). Other names in common use include imidazoleacetic hydroxylase, imidazoleacetate hydroxylase, and imidazoleacetic monooxygenase. This enzyme participates in histidine metabolism. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isoflavone%202%27-hydroxylase | In enzymology, an isoflavone 2'-hydroxylase (, Formerly ) is an enzyme that catalyzes the chemical reaction
an isoflavone + NADPH + H+ + O2 a 2'-hydroxyisoflavone + NADP+ + H2O
The 4 substrates of this enzyme are isoflavone, NADPH, H+, and O2, whereas its 3 products are 2'-hydroxyisoflavone, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is isoflavone,NADPH:oxygen oxidoreductase (2'-hydroxylating). Other names in common use include isoflavone 2'-monooxygenase, CYP81E1, and CYP Ge-3. This enzyme participates in isoflavonoid biosynthesis.
References
EC 1.14.14
NADPH-dependent enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/Isoflavone%203%27-hydroxylase | In enzymology, an isoflavone 3'-hydroxylase (, Formerly ) is an enzyme that catalyzes the chemical reaction
formononetin + NADPH + H+ + O2 calycosin + NADP+ + H2O
The 4 substrates of this enzyme are formononetin, NADPH, H+, and O2, whereas its 3 products are calycosin, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is formononetin,NADPH:oxygen oxidoreductase (3'-hydroxylating). This enzyme is also called isoflavone 3'-monooxygenase. This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.
References
EC 1.14.14
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/Juglone%203-monooxygenase | In enzymology, juglone 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
5-hydroxy-1,4-naphthoquinone + AH2 + O2 3,5-dihydroxy-1,4-naphthoquinone + A + H2O
The 3 substrates of this enzyme are 5-hydroxy-1,4-naphthoquinone, AH2, and O2, whereas its 3 products are 3,5-dihydroxy-1,4-naphthoquinone, A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O miscellaneous. The systematic name of this enzyme class is 5-hydroxy-1,4-naphthoquinone,hydrogen-donor:oxygen oxidoreductase (3-hydroxylating). Other names in common use include juglone hydroxylase, naphthoquinone hydroxylase, and naphthoquinone-hydroxylase.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Kynurenine%203-monooxygenase | In enzymology, a kynurenine 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
-kynurenine + NADPH + H+ + O2 3-hydroxy--kynurenine + NADP+ + H2O
Kynurenine 3-monooxygenase is the expression product of the KMO (gene). The systematic name of this enzyme class is -kynurenine, NADPH:oxygen oxidoreductase (3-hydroxylating). Other names in common use include kynurenine 3-hydroxylase, kynurenine hydroxylase, and -kynurenine-3-hydroxylase. It participates in tryptophan metabolism through the kynurenine catabolic pathway. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on paired donors, with O2 as the oxidant. Kynurenine 3-monooxygenase catalyzes the insertion of molecular oxygen into the aromatic ring of kynurenine to produce 3-hydroxy--kynurenine. It employs one cofactor, FAD. Kynurenine 3-monooxygenase serves as an important branch point in the kynurenine pathway and, as a result, is an attractive drug target for immunological, neurodegenerative, and neuroinflammatory diseases. Currently, most research on the kynurenine 3-monooxygenase enzyme has been focused primarily on rat models and in yeast, both of which have been demonstrated to have high sequence homology with the human kynurenine 3-monooxygenase protein. Studies have shown the beneficial effects of enzyme inhibition in these eukaryotic kynurenine 3-monooxygenase active sites, thus making this enzyme an attractive target for human drug design.
Structure
Kynurenine 3 |
https://en.wikipedia.org/wiki/Kynurenine%207%2C8-hydroxylase | In enzymology, a kynurenine 7,8-hydroxylase () is an enzyme that catalyzes the chemical reaction
kynurenate + AH2 + O2 7,8-dihydro-7,8-dihydroxykynurenate + A
The 3 substrates of this enzyme are kynurenate, an electron acceptor AH2, and O2, whereas its two products are 7,8-dihydro-7,8-dihydroxykynurenate and the reduction product A.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is oxidoreductase (hydroxylating). Other names in common use include kynurenic acid hydroxylase, kynurenic hydroxylase, and kynurenate 7,8-hydroxylase. This enzyme participates in tryptophan metabolism.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%CE%947-sterol%205%286%29-desaturase | {{DISPLAYTITLE:Δ7-sterol 5(6)-desaturase}}
In enzymology, a Δ7-sterol 5(6)-desaturase () is an enzyme that catalyzes the chemical reaction
Δ7-sterol + 2 ferrocytochrome b5 + + 2 H+ = Δ5,7-sterol + 2 ferricytochrome b5 + 2
The four substrates of this enzyme are Δ7-sterol, ferrocytochrome b5, H+, and O2. Its three products are Δ5,7-sterol, ferricytochrome b5, and H2O.
Classification
This enzyme is one of C-5 sterol desaturases, belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2. With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water.
Nomenclature
The systematic name of this enzyme class is Δ7-sterol,ferrocytochrome b5:oxygen oxidoreductase 5,6-dehydrogenating. Other names in common use include:
lathosterol oxidase
Δ7-sterol Δ5-dehydrogenase
Δ7-sterol 5-desaturase
Δ7-sterol-C5(6)-desaturase
5-DES
Gene names:
SC5D (vertebrates)
ERG3 (yeast)
Biological role
This enzyme participates in biosynthesis of steroids.
History
Previously, this enzyme was known under the name lathosterol oxidase and (), and the entry is now transferred. The following incorrect reaction was suggested:
5α-cholest-7-en-3β-ol + NAD(P)H + H+ + O2 cholesta-5,7-dien-3β-ol + NAD(P)+ + 2 H2O
The substrates of this enzyme were listed as 5α-cholest-7-en-3β-ol, NAD(P)H, H+, and O2. Its product |
https://en.wikipedia.org/wiki/Latia-luciferin%20monooxygenase%20%28demethylating%29 | In enzymology, a Latia-luciferin monooxygenase (demethylating) () is an enzyme that catalyzes the chemical reaction
Latia luciferin + AH2 + 2 O2 oxidized Latia luciferin + CO2 + formate + A + H2O + hnu
The 3 substrates of this enzyme are Latia luciferin, an electron acceptor AH2, and O2, whereas its 6 products are oxidized Latia luciferin, CO2, formate, the reduction product A, H2O, and hn.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is Latia-luciferin,hydrogen-donor:oxygen oxidoreductase (demethylating). Other names in common use include luciferase (Latia luciferin), and Latia luciferin monooxygenase (demethylating). It has 2 cofactors: FAD, and Flavoprotein.
References
EC 1.14.99
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Leucocyanidin%20oxygenase | In enzymology, a leucocyanidin oxygenase () is an enzyme that catalyzes the chemical reaction
leucocyanidin + 2-oxoglutarate + O2 cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O
The 3 substrates of this enzyme are leucocyanidin, 2-oxoglutarate, and O2, whereas its 5 products are cis-dihydroquercetin, trans-dihydroquercetin, succinate, CO2, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is leucocyanidin,2-oxoglutarate:oxygen oxidoreductase. This enzyme is also called leucoanthocyanidin dioxygenase (LDOX) or anthocyanidin synthase (ANS). This enzyme participates in flavonoid biosynthesis.
In a broader way, leucocyanidin oxygenase uses flavan-3,4-diols (leucoanthocyanidins) to produce 3-hydroxyanthocyanidins. The gene encoding the enzyme (PpLDOX) has been identified in peach and expression has been studied in Vitis vinifera.
Structural studies
As of late 2007, only one structure, in Arabidopsis thaliana, has been solved for this class of enzymes, with the PDB accession code .
References
Further reading
EC 1.14.11
Enzymes of known structure
Flavanonols metabolism |
https://en.wikipedia.org/wiki/Leukotriene-B4%2020-monooxygenase | In enzymology, a leukotriene-B4 20-monooxygenase () is an enzyme that catalyzes the chemical reaction
(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + H+ + O2 (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14- tetraenoate + NADP+ + H2O
The 4 substrates of this enzyme are (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate, NADPH, H+, and O2, whereas its 4 products are (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-, tetraenoate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate,N ADPH:oxygen oxidoreductase (20-hydroxylating). Other names in common use include leukotriene-B4 20-hydroxylase, leucotriene-B4 omega-hydroxylase, LTB4 20-hydroxylase, and LTB4 omega-hydroxylase. This enzyme participates in arachidonic acid metabolism. It employs one cofactor, heme.
References
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Leukotriene-E4%2020-monooxygenase | In enzymology, a leukotriene-E4 20-monooxygenase () is an enzyme that catalyzes the chemical reaction
(7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14- tetraenoate + NADPH + H+ + O2 20-hydroxyleukotriene E4 + NADP+ + H2O
The 5 substrates of this enzyme are (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-, tetraenoate, NADPH, H+, and O2, whereas its 3 products are 20-hydroxyleukotriene E4, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-te traenoate,NADPH:oxygen oxidoreductase (20-hydroxylating). This enzyme is also called leukotriene-E4 omega-hydroxylase. This enzyme participates in arachidonic acid metabolism.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Licodione%20synthase | In enzymology, a licodione synthase () is an enzyme that catalyzes the chemical reaction
liquiritigenin + NADPH + H+ + O2 licodione + NADP+ + H2O
The 4 substrates of this enzyme are liquiritigenin, NADPH, H+, and O2, whereas its 3 products are licodione, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is liquiritigenin,NADPH:oxygen oxidoreductase (licodione-forming).
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Linalool%208-monooxygenase | In enzymology, a linalool 8-monooxygenase (, Formerly ) is an enzyme that catalyzes the chemical reaction
3,7-dimethylocta-1,6-dien-3-ol + AH2 + O2 (E)-3,7-dimethylocta-1,6-dien-3,8-diol + A + H2O
The 3 substrates of this enzyme are 3,7-dimethylocta-1,6-dien-3-ol, an electron acceptor AH2, and O2, whereas its 3 products are (E)-3,7-dimethylocta-1,6-diene-3,8-diol, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is 3,7-dimethylocta-1,6-dien-3-ol,hydrogen-donor:oxygen oxidoreductase (8-hydroxylating). It employs one cofactor, heme.
References
EC 1.14.14
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Linoleoyl-CoA%20desaturase | In enzymology, a linoleoyl-CoA desaturase (also Delta 6 desaturase, ) is an enzyme that converts between types of fatty acids, which are essential nutrients in the human body. The enzyme mainly catalyzes the chemical reaction
linoleoyl-CoA + AH2 + O2 gamma-linolenoyl-CoA + A + 2 H2O
The 3 substrates of this enzyme are linoleoyl-CoA, an electron acceptor AH2, and O2, whereas its 3 products are gamma-linolenoyl-CoA, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with oxidation of a pair of donors resulting in the reduction of O to two molecules of water. The systematic name of this enzyme class is linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase. Other names in common use include acyl-CoA 6-desaturase, Delta6-desaturase (D6D or Δ-6-desaturase), Delta6-fatty acyl-CoA desaturase, Delta6-acyl CoA desaturase, fatty acid Delta6-desaturase, fatty acid 6-desaturase, linoleate desaturase, linoleic desaturase, linoleic acid desaturase, linoleoyl CoA desaturase, linoleoyl-coenzyme A desaturase, and long-chain fatty acid Delta6-desaturase. This enzyme participates in linoleic acid metabolism. It employs one cofactor, iron.
The enzyme is molecularly identical across all living things. It is present in animals, plants, fungi, and cyanobacteria.
D6D is one of the 3 fatty acid desaturase |
https://en.wikipedia.org/wiki/Lithocholate%206beta-hydroxylase | In enzymology, a lithocholate 6beta-hydroxylase () is an enzyme that catalyzes the chemical reaction
lithocholate + NADPH + H+ + O2 6beta-hydroxylithocholate + NADP+ + H2O
The 4 substrates of this enzyme are lithocholate, NADPH, H+, and O2, whereas its 3 products are 6beta-hydroxylithocholate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is lithocholate,NADPH:oxygen oxidoreductase (6beta-hydroxylating). Other names in common use include lithocholate 6beta-monooxygenase, CYP3A10, 6beta-hydroxylase, and cytochrome P450 3A10/lithocholic acid 6beta-hydroxylase.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-lysine%206-monooxygenase%20%28NADPH%29 | In enzymology, a L-lysine 6-monooxygenase (NADPH) () is an enzyme that catalyzes the chemical reaction
L-lysine + NADPH + H+ + O2 N6-hydroxy-L-lysine + NADP+ + H2O
The 4 substrates of this enzyme are L-lysine, NADPH, H+, and O2, whereas its 3 products are N6-hydroxy-L-lysine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is L-lysine,NADPH:oxygen oxidoreductase (6-hydroxylating). This enzyme is also called lysine N6-hydroxylase. This enzyme participates in lysine degradation.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mandelate%204-monooxygenase | In enzymology, a mandelate 4-monooxygenase () is an enzyme that catalyzes the chemical reaction
(S)-2-hydroxy-2-phenylacetate + tetrahydrobiopterin + O2 (S)-4-hydroxymandelate + dihydrobiopterin + H2O
The 3 substrates of this enzyme are (S)-2-hydroxy-2-phenylacetate, tetrahydrobiopterin, and O2, whereas its 3 products are (S)-4-hydroxymandelate, dihydrobiopterin, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced pteridine as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is (S)-2-hydroxy-2-phenylacetate,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating). Other names in common use include L-mandelate 4-hydroxylase, and mandelic acid 4-hydroxylase. It employs one cofactor, iron.
References
EC 1.14.16
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Melilotate%203-monooxygenase | In enzymology, a melilotate 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
The 4 substrates of this enzyme are 3-(2-hydroxyphenyl)propanoate, NADH, H+, and O2, whereas its 3 products are 3-(2,3-dihydroxyphenyl)propanoate, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 3-(2-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (3-hydroxylating). Other names in common use include 2-hydroxyphenylpropionate hydroxylase, melilotate hydroxylase, 2-hydroxyphenylpropionic hydroxylase, and melilotic hydroxylase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28-%29-menthol%20monooxygenase | In enzymology, a (−)-menthol monooxygenase () is an enzyme that catalyzes the chemical reaction
(−)-menthol + NADPH + H + O p-menthane-3,8-diol + NADP + HO
The 4 substrates of this enzyme are (−)-menthol, NADPH, H, and O, whereas its 3 products are p-menthane-3,8-diol, NADP, and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (−)-menthol,NADPH:oxygen oxidoreductase (8-hydroxylating). This enzyme is also called l-menthol monooxygenase.
Uses
Use of (−)-menthol monooxygenase has been explored by several companies including Procter & Gamble for cleaning products.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methyltetrahydroprotoberberine%2014-monooxygenase | In enzymology, a methyltetrahydroprotoberberine 14-monooxygenase () is an enzyme that catalyzes the chemical reaction
(S)-N-methylcanadine + NADPH + H+ + O2 allocryptopine + NADP+ + H2O
The 4 substrates of this enzyme are (S)-N-methylcanadine, NADPH, H+, and O2, whereas its 3 products are allocryptopine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (S)-N-methylcanadine,NADPH:oxygen oxidoreductase (14-hydroxylating). Other names in common use include methyltetrahydroprotoberberine 14-hydroxylase, (S)-cis-N-methyltetrahydroberberine 14-monooxygenase, and (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase. This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, heme.
References
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Monoprenyl%20isoflavone%20epoxidase | In enzymology, a monoprenyl isoflavone epoxidase () is an enzyme that catalyzes the chemical reaction
7-O-methylluteone + NADPH + H+ + O2 dihydrofurano derivatives + NADP+ + H2O
The 4 substrates of this enzyme are 7-O-methylluteone, NADPH, H+, and O2, whereas its 3 products are dihydrofurano pyranoisoflavone derivative, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is 7-O-methylluteone,NADPH:O2 oxidoreductase. Other names in common use include monoprenyl isoflavone monooxygenase, and 7-O-methylluteone:O2 oxidoreductase.
References
EC 1.14.99
NADPH-dependent enzymes
Enzymes of unknown structure
Isoflavones metabolism |
https://en.wikipedia.org/wiki/Myristoyl-CoA%2011-%28E%29%20desaturase | In enzymology, a myristoyl-CoA 11-(E) desaturase () is an enzyme that catalyzes the chemical reaction
myristoyl-CoA + NAD(P)H + H+ + O2 (E)-11-tetradecenoyl-CoA + NAD(P)+ + 2 H2O
The 5 substrates of this enzyme are myristoyl-CoA, NADH, NADPH, H+, and O2, whereas its 4 products are (E)-11-tetradecenoyl-CoA, NAD+, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O miscellaneous. The systematic name of this enzyme class is n-tetradecanoyl-CoA,NAD(P)H:O2 oxidoreductase [11-(E) desaturating].
References
EC 1.14.99
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Myristoyl-CoA%2011-%28Z%29%20desaturase | In enzymology, a myristoyl-CoA 11-(Z) desaturase () is an enzyme that catalyzes the chemical reaction
myristoyl-CoA + NAD(P)H + H+ + O2 (Z)-11-tetradecenoyl-CoA + NAD(P)+ + 2 H2O
The 5 substrates of this enzyme are myristoyl-CoA, NADH, NADPH, H+, and O2, whereas its 4 products are (Z)-11-tetradecenoyl-CoA, NAD+, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is n-tetradecanoyl-CoA,NAD(P)H:O2 oxidoreductase [11-(Z) desaturating]. This enzyme is also called n-tetradecanoyl-CoA,NADPH:O2 oxidoreductase [11-(Z) desaturating].
References
EC 1.14.99
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Naphthalene%201%2C2-dioxygenase | In enzymology, a naphthalene 1,2-dioxygenase () is an enzyme that catalyzes the chemical reaction
naphthalene + NADH + H+ + O2 (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
The 4 substrates of this enzyme are naphthalene, NADH, H+, and O2, whereas its two products are (1R,2S)-1,2-dihydronaphthalene-1,2-diol and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is naphthalene,NADH:oxygen oxidoreductase (1,2-hydroxylating). Other names in common use include naphthalene dioxygenase, and naphthalene oxygenase. This enzyme participates in 4 metabolic pathways: 1- and 2-methylnaphthalene degradation, naphthalene and anthracene degradation, fluorene degradation, and ethylbenzene degradation. It employs one cofactor, iron.
Structural studies
As of late 2007, 18 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , and .
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Iron enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nitric%20oxide%20dioxygenase | Nitric oxide dioxygenase () is an enzyme that catalyzes the conversion of nitric oxide (NO) to nitrate (NO)
. The net reaction for the reaction catalyzed by nitric oxide dioxygenase is shown below:
2NO + 2O2 + NAD(P)H → 2NO3− + NAD(P)+ + H+
Nitric oxide is a ubiquitous small molecule that is integrated in a wide variety of physiological processes including smooth muscle vasodilation, platelet disaggregation, neurotransmission, and immune response to bacterial infection. Overproduction of this signaling molecule can be lethal to cells by poisoning cellular energy production. The most sensitive targets of NO are aconitase, an enzyme that catalyzes the isomerization of citrate to isocitrate in the citric acid cycle, and cytochrome oxidase, the last enzyme in the respiratory electron transport chain of mitochondria. Additionally NO, with its lone radical on the nitrogen atom, is implicated in a number of secondary mechanisms of toxicity, including catalase inhibition (resulting in hydrogen peroxide toxicity), Fe-S center iron liberation, and the formation of dinitosyl-iron complexes.
Due to the potential lethality of NO, cells benefitted greatly from the evolution of an enzyme capable of catalyzing the conversion of toxic NO to nitrate.
A 'nitric oxide dioxygenase' is an enzyme that is capable of carrying out this reaction. NO dioxygenase belongs to the family of oxidoreductases, more specifically those acting on paired donors, with O2 as oxidant and with incorporation o |
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